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Volumn 63, Issue 5, 2007, Pages 1524-1536

Limited tolerance towards folded elements during secretion of the autotransporter Hbp

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DSBA PROTEIN; HEMOGLOBIN PROTEINASE; PROTEIN; PROTEIN DEGP; UNCLASSIFIED DRUG;

EID: 33847000902     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2007.05605.x     Document Type: Article
Times cited : (100)

References (46)
  • 1
    • 11844260767 scopus 로고    scopus 로고
    • Intimin-mediated export of passenger proteins requires maintenance of a translocation-competent conformation
    • Adams, T.M., Wentzel, A., and Kolmar, H. (2005) Intimin-mediated export of passenger proteins requires maintenance of a translocation-competent conformation. J Bacteriol 187: 522-533.
    • (2005) J Bacteriol , vol.187 , pp. 522-533
    • Adams, T.M.1    Wentzel, A.2    Kolmar, H.3
  • 2
    • 0035151832 scopus 로고    scopus 로고
    • Periplasmic transit and disulfide bond formation of the autotransported Shigella protein IcsA
    • Brandon, L.D., and Goldberg, M.B. (2001) Periplasmic transit and disulfide bond formation of the autotransported Shigella protein IcsA. J Bacteriol 183: 951-958.
    • (2001) J Bacteriol , vol.183 , pp. 951-958
    • Brandon, L.D.1    Goldberg, M.B.2
  • 4
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • DeLisa, M.P., Tullman, D., and Georgiou, G. (2003) Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc Natl Acad Sci USA 100: 6115-6120.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6115-6120
    • DeLisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 5
    • 0037244586 scopus 로고    scopus 로고
    • Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole
    • Den Blaauwen, T., Aarsman, M.E., Vischer, N.O., and Nanninga, N. (2003) Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole. Mol Microbiol 47: 539-547.
    • (2003) Mol Microbiol , vol.47 , pp. 539-547
    • Den Blaauwen, T.1    Aarsman, M.E.2    Vischer, N.O.3    Nanninga, N.4
  • 6
    • 0037189507 scopus 로고    scopus 로고
    • Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology
    • Desmyter, A., Spinelli, S., Payan, F., Lauwereys, M., Wyns, L., Muyldermans, S., and Cambillau, C. (2002) Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology. J Biol Chem 277: 23645-23650.
    • (2002) J Biol Chem , vol.277 , pp. 23645-23650
    • Desmyter, A.1    Spinelli, S.2    Payan, F.3    Lauwereys, M.4    Wyns, L.5    Muyldermans, S.6    Cambillau, C.7
  • 7
    • 0023187089 scopus 로고
    • Optimal posttranslational translocation of the precursor of PhoE protein across Escherichia coli membrane vesicles requires both ATP and the protonmotive force
    • De Vrije, T., Tommassen, J., and De Kruijff, B. (1987) Optimal posttranslational translocation of the precursor of PhoE protein across Escherichia coli membrane vesicles requires both ATP and the protonmotive force. Biochem Biophys Acta 900: 63-72.
    • (1987) Biochem Biophys Acta , vol.900 , pp. 63-72
    • De Vrije, T.1    Tommassen, J.2    De Kruijff, B.3
  • 9
    • 0034783458 scopus 로고    scopus 로고
    • Outer membrane targeting of passenger proteins by the vacuolating cytotoxin autotransporter of Helicobacter pylori
    • Fischer, W., Buhrdorf, R., Gerland, E., and Haas, R. (2001) Outer membrane targeting of passenger proteins by the vacuolating cytotoxin autotransporter of Helicobacter pylori. Infect Immun 69: 6769-6775.
    • (2001) Infect Immun , vol.69 , pp. 6769-6775
    • Fischer, W.1    Buhrdorf, R.2    Gerland, E.3    Haas, R.4
  • 10
    • 0021114573 scopus 로고
    • Influence of temperature and denaturing agents on the structural stability of calmodulin. A 1H-nuclear magnetic resonance study
    • Guerini, D., and Krebs, J. (1983) Influence of temperature and denaturing agents on the structural stability of calmodulin. A 1H-nuclear magnetic resonance study. FEBS Lett 164: 105-110.
    • (1983) FEBS Lett , vol.164 , pp. 105-110
    • Guerini, D.1    Krebs, J.2
  • 11
    • 0031764411 scopus 로고    scopus 로고
    • Importance of using lac rather than ara promoter vectors for modulating the levels of toxic gene products in Escherichia coli. [Letter]
    • Hashemzadeh-Bonehi, L., Mehraein-Ghomi, F., Mitsopoulos, C., Jacob, J.P., Hennessey, E.S., and Broome-Smith, J.K. (1998) Importance of using lac rather than ara promoter vectors for modulating the levels of toxic gene products in Escherichia coli. [Letter]. Mol Microbiol 30: 676-678.
    • (1998) Mol Microbiol , vol.30 , pp. 676-678
    • Hashemzadeh-Bonehi, L.1    Mehraein-Ghomi, F.2    Mitsopoulos, C.3    Jacob, J.P.4    Hennessey, E.S.5    Broome-Smith, J.K.6
  • 12
    • 0024046835 scopus 로고
    • Model building of disulfide bonds in proteins with known three-dimensional structure
    • Hazes, B., and Dijkstra, B.W. (1988) Model building of disulfide bonds in proteins with known three-dimensional structure. Protein Eng 2: 119-125.
    • (1988) Protein Eng , vol.2 , pp. 119-125
    • Hazes, B.1    Dijkstra, B.W.2
  • 13
    • 0035111746 scopus 로고    scopus 로고
    • Virulence functions of autotransporter proteins
    • Henderson, I.R., and Nataro, J.P. (2001) Virulence functions of autotransporter proteins. Infect Immun 69: 1231-1243.
    • (2001) Infect Immun , vol.69 , pp. 1231-1243
    • Henderson, I.R.1    Nataro, J.P.2
  • 15
    • 8844235655 scopus 로고    scopus 로고
    • Protein secretion through autotransporter and two-partner pathways
    • Jacob-Dubuisson, F., Fernandez, R., and Coutte, L. (2004) Protein secretion through autotransporter and two-partner pathways. Biochim Biophys Acta 1694: 235-257.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 235-257
    • Jacob-Dubuisson, F.1    Fernandez, R.2    Coutte, L.3
  • 16
    • 21344432762 scopus 로고    scopus 로고
    • Autodisplay of the protease inhibitor aprotinin in Escherichia coli
    • Jose, J., and Zangen, D. (2005) Autodisplay of the protease inhibitor aprotinin in Escherichia coli. Biochem Biophys Res Commun 333: 1218-1226.
    • (2005) Biochem Biophys Res Commun , vol.333 , pp. 1218-1226
    • Jose, J.1    Zangen, D.2
  • 17
    • 0030608368 scopus 로고    scopus 로고
    • Absence of periplasmic DsbA oxidoreductase facilitates export of cysteine-containing passenger proteins to the Escherichia coli cell surface via the Iga beta autotransporter pathway
    • Jose, J., Kramer, J., Klauser, T., Pohlner, J., and Meyer, T.F. (1996) Absence of periplasmic DsbA oxidoreductase facilitates export of cysteine-containing passenger proteins to the Escherichia coli cell surface via the Iga beta autotransporter pathway. Gene 178: 107-110.
    • (1996) Gene , vol.178 , pp. 107-110
    • Jose, J.1    Kramer, J.2    Klauser, T.3    Pohlner, J.4    Meyer, T.F.5
  • 18
    • 0025353145 scopus 로고
    • Extracellular transport of cholera toxin B subunit using Neisseria IgA protease beta-domain: Conformation-dependent outer membrane translocation
    • Klauser, T., Pohlner, J., and Meyer, T.F. (1990) Extracellular transport of cholera toxin B subunit using Neisseria IgA protease beta-domain: conformation-dependent outer membrane translocation. EMBO J 9: 1991-1999.
    • (1990) EMBO J , vol.9 , pp. 1991-1999
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 19
    • 0026511122 scopus 로고
    • Selective extracellular release of cholera toxin B subunit by Escherichia coli: Dissection of Neisseria Iga beta-mediated outer membrane transport
    • Klauser, T., Pohlner, J., and Meyer, T.F. (1992) Selective extracellular release of cholera toxin B subunit by Escherichia coli: dissection of Neisseria Iga beta-mediated outer membrane transport. EMBO J 11: 2327-2335.
    • (1992) EMBO J , vol.11 , pp. 2327-2335
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 20
    • 0034015838 scopus 로고    scopus 로고
    • Cell surface presentation of recombinant (poly-) peptides including functional T-cell epitopes by the AIDA autotransporter system
    • Konieczny, M.P., Suhr, M., Noll, A., Autenrieth, I.B., and Alexander Schmidt, M. (2000) Cell surface presentation of recombinant (poly-) peptides including functional T-cell epitopes by the AIDA autotransporter system. FEMS Immunol Med Microbiol 27: 321-332.
    • (2000) FEMS Immunol Med Microbiol , vol.27 , pp. 321-332
    • Konieczny, M.P.1    Suhr, M.2    Noll, A.3    Autenrieth, I.B.4    Alexander Schmidt, M.5
  • 21
    • 0034051291 scopus 로고    scopus 로고
    • Autodisplay: Functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter
    • Lattemann, C.T., Maurer, J., Gerland, E., and Meyer, T.F. (2000) Autodisplay: functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter. J Bacteriol 182: 3726-3733.
    • (2000) J Bacteriol , vol.182 , pp. 3726-3733
    • Lattemann, C.T.1    Maurer, J.2    Gerland, E.3    Meyer, T.F.4
  • 22
    • 33646784690 scopus 로고    scopus 로고
    • Paired cysteine residues are required for high levels of the Helicobacter pylori autotransporter VacA
    • Letley, D.P., Rhead, J.L., Bishop, K., and Atherton, J.C. (2006) Paired cysteine residues are required for high levels of the Helicobacter pylori autotransporter VacA. Microbiology 152: 1319-1325.
    • (2006) Microbiology , vol.152 , pp. 1319-1325
    • Letley, D.P.1    Rhead, J.L.2    Bishop, K.3    Atherton, J.C.4
  • 23
    • 0031034089 scopus 로고    scopus 로고
    • Autodisplay: One-component system for efficient surface display and release of soluble recombinant proteins from Escherichia coli
    • Maurer, J., Jose, J., and Meyer, T.F. (1997) Autodisplay: one-component system for efficient surface display and release of soluble recombinant proteins from Escherichia coli. J Bacteriol 179: 794-804.
    • (1997) J Bacteriol , vol.179 , pp. 794-804
    • Maurer, J.1    Jose, J.2    Meyer, T.F.3
  • 24
    • 33745743311 scopus 로고    scopus 로고
    • Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter
    • Meng, G., Surana, N.K., St Geme, J.W., III, and Waksman, G. (2006) Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter. EMBO J 25: 2297-2304.
    • (2006) EMBO J , vol.25 , pp. 2297-2304
    • Meng, G.1    Surana, N.K.2    St Geme III, J.W.3    Waksman, G.4
  • 25
    • 0037205935 scopus 로고    scopus 로고
    • Characterization and crystal structure of a high-affinity pentavalent receptor-binding inhibitor for cholera toxin and E. coli heat-labile enterotoxin
    • Merritt, E.A., Zhang, Z., Pickens, J.C., Ahn, M., Hol, W.G., and Fan, E. (2002) Characterization and crystal structure of a high-affinity pentavalent receptor-binding inhibitor for cholera toxin and E. coli heat-labile enterotoxin. J Am Chem Soc 124: 8818-8824.
    • (2002) J Am Chem Soc , vol.124 , pp. 8818-8824
    • Merritt, E.A.1    Zhang, Z.2    Pickens, J.C.3    Ahn, M.4    Hol, W.G.5    Fan, E.6
  • 26
    • 33846992061 scopus 로고    scopus 로고
    • Miller, J.H. (1992) A Short Course in Bacterial Genetics; A Laboratory Manual and Handbook For Escherichia coli and Related Bacteria. New York: Cold Spring Harbor Laboratory Press.
    • Miller, J.H. (1992) A Short Course in Bacterial Genetics; A Laboratory Manual and Handbook For Escherichia coli and Related Bacteria. New York: Cold Spring Harbor Laboratory Press.
  • 27
    • 33646550516 scopus 로고    scopus 로고
    • Proteomic analysis of extracellular proteins from Escherichia coli W3110
    • Nandakumar, M.P., Cheung, A., and Marten, M.R. (2006) Proteomic analysis of extracellular proteins from Escherichia coli W3110. J Proteome Res 5: 1155-1161.
    • (2006) J Proteome Res , vol.5 , pp. 1155-1161
    • Nandakumar, M.P.1    Cheung, A.2    Marten, M.R.3
  • 28
    • 0037338681 scopus 로고    scopus 로고
    • A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain
    • Oliver, D.C., Huang, G., Nodel, E., Pleasance, S., and Fernandez, R.C. (2003) A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain. Mol Microbiol 47: 1367-1383.
    • (2003) Mol Microbiol , vol.47 , pp. 1367-1383
    • Oliver, D.C.1    Huang, G.2    Nodel, E.3    Pleasance, S.4    Fernandez, R.C.5
  • 29
  • 30
    • 0032555939 scopus 로고    scopus 로고
    • Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli EB1
    • Otto, B.R., van Dooren, S.J.M., Nuijens, J.H., Luirink, J., and Oudega, B. (1998) Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli EB1. J Exp Med 188: 1091-1103.
    • (1998) J Exp Med , vol.188 , pp. 1091-1103
    • Otto, B.R.1    van Dooren, S.J.M.2    Nuijens, J.H.3    Luirink, J.4    Oudega, B.5
  • 31
    • 0036139096 scopus 로고    scopus 로고
    • Escherichia coli hemoglobin protease autotransporter contributes to synergistic abscess formation and heme-dependent growth of Bacteroides fragilis
    • Otto, B.R., van Dooren, S.J., Dozois, C.M., Luirink, J., and Oudega, B. (2002) Escherichia coli hemoglobin protease autotransporter contributes to synergistic abscess formation and heme-dependent growth of Bacteroides fragilis. Infect Immun 70: 5-10.
    • (2002) Infect Immun , vol.70 , pp. 5-10
    • Otto, B.R.1    van Dooren, S.J.2    Dozois, C.M.3    Luirink, J.4    Oudega, B.5
  • 32
    • 20444435483 scopus 로고    scopus 로고
    • Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli
    • Otto, B.R., Sijbrandi, R., Luirink, J., Oudega, B., Heddle, J.G., Mizutani, K., et al. (2005) Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli. J Biol Chem 280: 17339-17345.
    • (2005) J Biol Chem , vol.280 , pp. 17339-17345
    • Otto, B.R.1    Sijbrandi, R.2    Luirink, J.3    Oudega, B.4    Heddle, J.G.5    Mizutani, K.6
  • 33
    • 0036839640 scopus 로고    scopus 로고
    • Shigella flexneri DegP facilitates IcsA surface expression and is required for efficient intercellular spread
    • Purdy, G.E., Hong, M., and Payne, S.M. (2002) Shigella flexneri DegP facilitates IcsA surface expression and is required for efficient intercellular spread. Infect Immun 70: 6355-6364.
    • (2002) Infect Immun , vol.70 , pp. 6355-6364
    • Purdy, G.E.1    Hong, M.2    Payne, S.M.3
  • 34
    • 0034770083 scopus 로고    scopus 로고
    • Roles of thiol-redox pathways in bacteria
    • Ritz, D., and Beckwith, J. (2001) Roles of thiol-redox pathways in bacteria. Annu Rev Microbiol 55: 21-48.
    • (2001) Annu Rev Microbiol , vol.55 , pp. 21-48
    • Ritz, D.1    Beckwith, J.2
  • 35
    • 15744389448 scopus 로고    scopus 로고
    • Sensing external stress: Watchdogs of the Escherichia coli cell envelope
    • Ruiz, N., and Silhavy, T.J. (2005) Sensing external stress: watchdogs of the Escherichia coli cell envelope. Curr Opin Microbiol 8: 122-126.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 122-126
    • Ruiz, N.1    Silhavy, T.J.2
  • 36
    • 33744746602 scopus 로고    scopus 로고
    • The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation
    • Rutherford, N., Charbonneau, M.E., Berthiaume, F., Betton, J.M., and Mourez, M. (2006) The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation. J Bacteriol 188:4111-4116.
    • (2006) J Bacteriol , vol.188 , pp. 4111-4116
    • Rutherford, N.1    Charbonneau, M.E.2    Berthiaume, F.3    Betton, J.M.4    Mourez, M.5
  • 37
    • 0037799238 scopus 로고    scopus 로고
    • Signal recognition particle (SRP)-mediated targeting and Sec-dependent translocation of an extracellular Escherichia coli protein
    • Sijbrandi, R., Urbanus, M.L., Ten Hagen-Jongman, C.M., Bernstein, H.D., Oudega, B., Otto, B.R., and Luirink, J. (2003) Signal recognition particle (SRP)-mediated targeting and Sec-dependent translocation of an extracellular Escherichia coli protein. J Biol Chem 278: 4654-4659.
    • (2003) J Biol Chem , vol.278 , pp. 4654-4659
    • Sijbrandi, R.1    Urbanus, M.L.2    Ten Hagen-Jongman, C.M.3    Bernstein, H.D.4    Oudega, B.5    Otto, B.R.6    Luirink, J.7
  • 38
    • 27944445725 scopus 로고    scopus 로고
    • Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter
    • Skillman, K.M., Barnard, T.J., Peterson, J.H., Ghirlando, R., and Bernstein, H.D. (2005) Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter. Mol Microbiol 58: 945-958.
    • (2005) Mol Microbiol , vol.58 , pp. 945-958
    • Skillman, K.M.1    Barnard, T.J.2    Peterson, J.H.3    Ghirlando, R.4    Bernstein, H.D.5
  • 39
    • 0023974826 scopus 로고
    • An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins
    • Strauch, K.L., and Beckwith, J. (1988) An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. Proc Natl Acad Sci USA 85: 1576-1580.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1576-1580
    • Strauch, K.L.1    Beckwith, J.2
  • 40
    • 0029621229 scopus 로고
    • Extracellular transport of VirG protein in Shigella
    • Suzuki, T., Lett, M.C., and Sasakawa, C. (1995) Extracellular transport of VirG protein in Shigella. J Biol Chem 270: 30874-30880.
    • (1995) J Biol Chem , vol.270 , pp. 30874-30880
    • Suzuki, T.1    Lett, M.C.2    Sasakawa, C.3
  • 41
    • 11844280919 scopus 로고    scopus 로고
    • An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter
    • Szabady, R.L., Peterson, J.H., Skillman, K.M., and Bernstein, H.D. (2005) An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter. Proc Natl Acad Sci USA 102: 221-226.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 221-226
    • Szabady, R.L.1    Peterson, J.H.2    Skillman, K.M.3    Bernstein, H.D.4
  • 42
    • 0036565670 scopus 로고    scopus 로고
    • Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains
    • Veiga, E., Sugawara, E., Nikaido, H., de Lorenzo, V., and Fernandez, L.A. (2002) Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains. EMBO J 21: 2122-2131.
    • (2002) EMBO J , vol.21 , pp. 2122-2131
    • Veiga, E.1    Sugawara, E.2    Nikaido, H.3    de Lorenzo, V.4    Fernandez, L.A.5
  • 43
    • 3142680440 scopus 로고    scopus 로고
    • Structural tolerance of bacterial autotransporters for folded passenger protein domains
    • Veiga, E., de Lorenzo, V., and Fernandez, L.A. (2004) Structural tolerance of bacterial autotransporters for folded passenger protein domains. Mol Microbiol 52: 1069-1080.
    • (2004) Mol Microbiol , vol.52 , pp. 1069-1080
    • Veiga, E.1    de Lorenzo, V.2    Fernandez, L.A.3
  • 44
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux, R., Bos, M.P., Geurtsen, J., Mols, M., and Tommassen, J. (2003) Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299: 262-265.
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 45
    • 2442442119 scopus 로고    scopus 로고
    • Directed in vitro evolution and crystallographic analysis of a peptide-binding single chain antibody fragment (scFv) with low picomolar affinity
    • Zahnd, C., Spinelli, S., Luginbuhl, B., Amstutz, P., Cambillau, C., and Pluckthun, A. (2004) Directed in vitro evolution and crystallographic analysis of a peptide-binding single chain antibody fragment (scFv) with low picomolar affinity. J Biol Chem 279: 18870-18877.
    • (2004) J Biol Chem , vol.279 , pp. 18870-18877
    • Zahnd, C.1    Spinelli, S.2    Luginbuhl, B.3    Amstutz, P.4    Cambillau, C.5    Pluckthun, A.6
  • 46
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang, M., Tanaka, T., and Ikura, M. (1995) Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat Struct Biol 2: 758-767.
    • (1995) Nat Struct Biol , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3


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